TGS1_SCHPO
ID TGS1_SCHPO Reviewed; 239 AA.
AC Q09814; P78826; Q9P7B6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Trimethylguanosine synthase;
DE EC=2.1.1.- {ECO:0000269|PubMed:15590684};
DE AltName: Full=Cap-specific guanine-N2 methyltransferase;
DE AltName: Full=snRNA/snoRNA cap hypermethylase;
GN Name=tgs1; ORFNames=SPAC2G11.15c, SPAC521.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=15590684; DOI=10.1074/jbc.c400554200;
RA Hausmann S., Shuman S.;
RT "Specificity and mechanism of RNA cap guanine-N2 methyltransferase
RT (Tgs1).";
RL J. Biol. Chem. 280:4021-4024(2005).
CC -!- FUNCTION: Catalyzes the two serial methylation steps for the conversion
CC of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a
CC 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is
CC specific for guanine, and N7 methylation must precede N2 methylation.
CC Required for pre-mRNA splicing, pre-rRNA processing and small ribosomal
CC subunit synthesis. Involved in nucleolar structural organization.
CC {ECO:0000269|PubMed:15590684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67620, Rhea:RHEA-COMP:17167, Rhea:RHEA-
CC COMP:17315, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156461, ChEBI:CHEBI:172880;
CC Evidence={ECO:0000269|PubMed:15590684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67621;
CC Evidence={ECO:0000269|PubMed:15590684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-
CC ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end
CC (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in
CC mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67624,
CC Rhea:RHEA-COMP:17171, Rhea:RHEA-COMP:17315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623,
CC ChEBI:CHEBI:172880; Evidence={ECO:0000269|PubMed:15590684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67625;
CC Evidence={ECO:0000269|PubMed:15590684};
CC -!- ACTIVITY REGULATION: Substrate inhibited by S-adenosyl-L-homocysteine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 mM for m(7)GDP {ECO:0000269|PubMed:15590684};
CC KM=8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:15590684};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15590684};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15590684}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC Trimethylguanosine synthase family. {ECO:0000305}.
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DR EMBL; D89174; BAA13836.1; -; mRNA.
DR EMBL; CU329670; CAA91180.1; -; Genomic_DNA.
DR PIR; T38581; T38581.
DR PIR; T42539; T42539.
DR RefSeq; NP_593095.3; NM_001018493.3.
DR AlphaFoldDB; Q09814; -.
DR SMR; Q09814; -.
DR BioGRID; 278498; 6.
DR IntAct; Q09814; 1.
DR STRING; 4896.SPAC2G11.15c.1; -.
DR MaxQB; Q09814; -.
DR PaxDb; Q09814; -.
DR EnsemblFungi; SPAC2G11.15c.1; SPAC2G11.15c.1:pep; SPAC2G11.15c.
DR GeneID; 2542015; -.
DR KEGG; spo:SPAC2G11.15c; -.
DR PomBase; SPAC2G11.15c; tgs1.
DR VEuPathDB; FungiDB:SPAC2G11.15c; -.
DR eggNOG; KOG2730; Eukaryota.
DR HOGENOM; CLU_029658_0_1_1; -.
DR InParanoid; Q09814; -.
DR OMA; LACAKHN; -.
DR PhylomeDB; Q09814; -.
DR PRO; PR:Q09814; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071164; F:RNA trimethylguanosine synthase activity; IDA:PomBase.
DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; IMP:PomBase.
DR GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF09445; Methyltransf_15; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..239
FT /note="Trimethylguanosine synthase"
FT /id="PRO_0000116412"
FT CONFLICT 193
FT /note="P -> A (in Ref. 1; BAA13836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 27157 MW; 4ADAF9FDB6F8CFF4 CRC64;
MNKNEELDED ELLKKCIICP PVPKALKKYW NNRYNLFSRF DEGIWLDYQS WYSVTPEKVA
VAIAKSVVDF IQPELIIDAF SGCGGNTIQF AKYCPVISIE IDPIKIAMAK HNLEIYGIPS
SRVTFIQGDV LDTFKSLQFA KDYRSLVFMS PPWGGPSYSG KTVYSLNDLN PYAFDVLFKE
ATRISPYVAA FLPRNTDVKE LAAYGSIHNK PYITNFLFEG YAKAICCYFN MKGAIARKI
